ID   OSTCN_HALDD             Reviewed;          19 AA.
AC   P83473;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Osteocalcin;
DE   AltName: Full=Bone Gla protein;
DE            Short=BGP;
DE   AltName: Full=Gamma-carboxyglutamic acid-containing protein;
DE   Flags: Fragment;
GN   Name=bglap;
OS   Halobatrachus didactylus (Lusitanian toadfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Batrachoidaria; Batrachoididae; Halobatrachus.
OX   NCBI_TaxID=101187;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND GAMMA-CARBOXYGLUTAMATION AT GLU-11; GLU-15 AND
RP   GLU-18.
RC   TISSUE=Cartilage;
RX   PubMed=14668966; DOI=10.1007/s00223-003-0079-4;
RA   Simes D.C., Williamson M.K., Schaff B.J., Gavaia P.J., Ingleton P.M.,
RA   Price P.A., Cancela M.L.;
RT   "Characterization of osteocalcin (BGP) and matrix Gla protein (MGP) fish
RT   specific antibodies: validation for immunodetection studies in lower
RT   vertebrates.";
RL   Calcif. Tissue Int. 74:170-180(2004).
CC   -!- FUNCTION: Binds strongly to apatite and calcium. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent
CC       carboxylation. These residues are essential for the binding of calcium.
CC       {ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:14668966,
CC       ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P83473; -.
DR   GO; GO:0031012; C:extracellular matrix; TAS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030282; P:bone mineralization; TAS:UniProtKB.
PE   1: Evidence at protein level;
KW   Biomineralization; Calcium; Direct protein sequencing;
KW   Gamma-carboxyglutamic acid; Metal-binding; Secreted.
FT   CHAIN           1..>19
FT                   /note="Osteocalcin"
FT                   /id="PRO_0000148909"
FT   DOMAIN          1..>19
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000305"
FT   BINDING         11
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         15
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         18
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         18
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:14668966"
FT   MOD_RES         15
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:14668966"
FT   MOD_RES         18
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:14668966"
FT   NON_TER         19
FT                   /evidence="ECO:0000303|PubMed:14668966"
SQ   SEQUENCE   19 AA;  2088 MW;  E15426C26B3E861C CRC64;
     AAAELSLVQL ESLREVCEQ